[Acid and alkaline denaturation of superoxide dismutase].

Title[Acid and alkaline denaturation of superoxide dismutase].
Publication TypeJournal Article
Year of Publication1975
AuthorsSimonian MA, Nalbandian RM
JournalBiofizika
Volume20
Issue5
Pagination783-7
Date Published1975 Sep-Oct
ISSN0006-3029
KeywordsAnimals, Cattle, Erythrocytes, Hydrogen-Ion Concentration, In Vitro Techniques, Protein Denaturation, Superoxide Dismutase
Abstract

Optical and ESR spectra of erythrocyte superoxide dismutase denaturated with acid and alkali are described. Sharp changes in activity and spectra were found. "Residual" activity of alkaline denaturated protein was higher than of acidic denaturated sample. It is suggested that covalent bonding copper-nitrogen is essential for superoxide dismutase activity of the protein or synthetic copper complexes.

Alternate JournalBiofizika
PubMed ID1099